ArticleThe Journal of biological chemistry2016
Scorpion Potassium Channel-blocking Defensin Highlights a Functional Link with Neurotoxin.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Scorpion Peptides in Antiviral Drug Discovery: An In-depth Review.Probiotics and antimicrobial proteins · 2026Review
- Transcriptomic analysis reveals members and expression characteristics of innate immunity genes in Chinese scorpion Mesobuthus martensii.Scientific reports · 2026Article
- Nanomaterials as electrochemical regulators of bacterial biofilms through the modulation of extracellular electron transport and ion channels.Journal of nanobiotechnology · 2026Review
- From venom peptides to neurotherapeutics: BmK defensins and short-chain peptides as modulators of ion channels.Frontiers in pharmacology · 2026Review
- Trans-kingdom conservation of mechanism between bacterial actifensin and eukaryotic defensins.npj antimicrobials and resistance · 2025Article
- Activity of Potassium Channel BmK-NSPK Inhibitor Regulated by Basic Amino Acid Residues: Novel Insight into the Diverse Peptide Pharmacology.Molecules (Basel, Switzerland) · 2025Article
- Antimicrobial Potential of Scorpion-Venom-Derived Peptides.Molecules (Basel, Switzerland) · 2024Review
- Unveiling mechanisms of antimicrobial peptide: Actions beyond the membranes disruption.Heliyon · 2024Review
- Peptides with Diverse Functions from Scorpion Venom: A Great Opportunity for the Treatment of a Wide Variety of Diseases.Iranian biomedical journal · 2023Article
- Use of Defensins to Develop Eco-Friendly Alternatives to Synthetic Fungicides to Control Phytopathogenic Fungi and Their Mycotoxins.Journal of fungi (Basel, Switzerland) · 2022Review
- Article
- Armed stem to stinger: a review of the ecological roles of scorpion weapons.The journal of venomous animals and toxins including tropical diseases · 2021Review
- Pigs Overexpressing Porcine β-Defensin 2 Display Increased Resilience toAntibiotics (Basel, Switzerland) · 2020Article
- Inhibitory Activity of a Scorpion Defensin BmKDfsin3 against Hepatitis C Virus.Antibiotics (Basel, Switzerland) · 2020Article
- The Dichotomous Responses Driven by β-Defensins.Frontiers in immunology · 2020Review
- Article
- Kv1.3 Channel as a Key Therapeutic Target for Neuroinflammatory Diseases: State of the Art and Beyond.Frontiers in neuroscience · 2019Review
- Mouse β-Defensin 3, A Defensin Inhibitor of Both Its Endogenous and Exogenous Potassium Channels.Molecules (Basel, Switzerland) · 2018Article
- Histidine-rich Modification of a Scorpion-derived Peptide Improves Bioavailability and Inhibitory Activity against HSV-1.Theranostics · 2018Article
- Molecular characterization and expression analysis of CSαβ defensin genes from the scorpionBioscience reports · 2017Article
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9 authors.
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Abstract
The structural similarity between defensins and scorpion neurotoxins suggests that they might have evolved from a common ancestor. However, there is no direct experimental evidence demonstrating a functional link between scorpion neurotoxins and defensins. The scorpion defensin BmKDfsin4 from Mesobuthus martensiiKarsch contains 37 amino acid residues and a conserved cystine-stabilized α/β structural fold. The recombinant BmKDfsin4, a classical defensin, has been found to have inhibitory activity against Gram-positive bacteria such as Staphylococcus aureus, Bacillus subtilis, and Micrococcus luteusas well as methicillin-resistant Staphylococcus aureus Interestingly, electrophysiological experiments showed that BmKDfsin4,like scorpion potassium channel neurotoxins, could effectively inhibit Kv1.1, Kv1.2, and Kv1.3 channel currents, and its IC50value for the Kv1.3 channel was 510.2 nm Similar to the structure-function relationships of classical scorpion potassium channel-blocking toxins, basic residues (Lys-13 and Arg-19) of BmKDfsin4 play critical roles in peptide-Kv1.3 channel interactions. Furthermore, mutagenesis and electrophysiological experiments demonstrated that the channel extracellular pore region is the binding site of BmKDfsin4, indicating that BmKDfsin4 adopts the same mechanism for blocking potassium channel currents as classical scorpion toxins. Taken together, our work identifies scorpion BmKDfsin4 as the first invertebrate defensin to block potassium channels. These findings not only demonstrate that defensins from invertebrate animals are a novel type of potassium channel blockers but also provide evidence of a functional link between defensins and neurotoxins.
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